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Database: UniProt
Entry: I1VBD5_9CRUS
LinkDB: I1VBD5_9CRUS
Original site: I1VBD5_9CRUS 
ID   I1VBD5_9CRUS            Unreviewed;       280 AA.
AC   I1VBD5;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   SubName: Full=Scavenger 4 {ECO:0000313|EMBL:AFI40099.1};
DE   Flags: Fragment;
OS   Daphnia parvula.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC   Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX   NCBI_TaxID=132684 {ECO:0000313|EMBL:AFI40099.1};
RN   [1] {ECO:0000313|EMBL:AFI40099.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C60 {ECO:0000313|EMBL:AFI40099.1};
RX   PubMed=22577801; DOI=10.1186/1471-2148-12-63;
RA   McTaggart S.J., Obbard D.J., Conlon C., Little T.J.;
RT   "Immune genes undergo more adaptive evolution than non-immune system genes
RT   in Daphnia pulex.";
RL   BMC Evol. Biol. 12:63-63(2012).
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00124}.
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DR   EMBL; JQ856753; AFI40099.1; -; mRNA.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   CDD; cd00112; LDLa; 1.
DR   Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 1.
DR   Gene3D; 3.10.250.10; SRCR-like domain; 2.
DR   InterPro; IPR036055; LDL_receptor-like_sf.
DR   InterPro; IPR023415; LDLR_class-A_CS.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   InterPro; IPR001190; SRCR.
DR   InterPro; IPR017448; SRCR-like_dom.
DR   InterPro; IPR036772; SRCR-like_dom_sf.
DR   PANTHER; PTHR48071:SF18; LCCL/LECTIN ADHESIVE-LIKE PROTEIN 1; 1.
DR   PANTHER; PTHR48071; SRCR DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00057; Ldl_recept_a; 1.
DR   Pfam; PF00530; SRCR; 2.
DR   PRINTS; PR00258; SPERACTRCPTR.
DR   SMART; SM00192; LDLa; 1.
DR   SMART; SM00202; SR; 2.
DR   SUPFAM; SSF57424; LDL receptor-like module; 1.
DR   SUPFAM; SSF56487; SRCR-like; 2.
DR   PROSITE; PS01209; LDLRA_1; 1.
DR   PROSITE; PS50068; LDLRA_2; 1.
DR   PROSITE; PS50287; SRCR_2; 2.
PE   2: Evidence at transcript level;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00196}; Hydrolase {ECO:0000256|ARBA:ARBA00022825};
KW   Protease {ECO:0000256|ARBA:ARBA00022825};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT   DOMAIN          1..84
FT                   /note="SRCR"
FT                   /evidence="ECO:0000259|PROSITE:PS50287"
FT   DOMAIN          133..233
FT                   /note="SRCR"
FT                   /evidence="ECO:0000259|PROSITE:PS50287"
FT   DISULFID        9..73
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT   DISULFID        22..83
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT   DISULFID        53..63
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT   DISULFID        158..222
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT   DISULFID        171..232
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT   DISULFID        202..212
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AFI40099.1"
FT   NON_TER         280
FT                   /evidence="ECO:0000313|EMBL:AFI40099.1"
SQ   SEQUENCE   280 AA;  30071 MW;  E2B2CC78BDBED5C5 CRC64;
     VFGXWGAICD DHFSANDANV ICRQLGFPLG ASQALSHSTF GPGSPILMDD VMCRGNETSL
     ADCPFAGWGV HNCAPEETAG VRCILAETTC TENQFKCETT DACIAIDFLC DTVDDCGDHS
     DENRTRCASE LLVRLADGPD SLSGRVELRQ NGIWGTVCDD DFGQEEATVI CRMLNLNGPA
     QPAKSGSFGP GKGPIWLDEL GCSGTENTLM ECARLPWAKH NCRHTEDAGV RCSHPTNEXK
     XPEDVTETNP VSTLTDLVQL GSLPVKCGIR MVEDNPSDPL
//
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